Opening book details…
Can I read Substrate Specificity and Regulation of Activity of Rat Liver β-D-Glucuronidase on EtoBox?
Substrate Specificity and Regulation of Activity of Rat Liver β-D-Glucuronidase by Reinhard NIEMANN; Eckhart BUDDECKE is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.
What is Substrate Specificity and Regulation of Activity of Rat Liver β-D-Glucuronidase about?
Highly purified rat liver --glucuronidase catalyses the hydrolysis of natural and synthetic j3-D-glucuronides. At pH 4 a release of glucuronic acid from chondroitin sulfate tetrasaccharide (GlcUA-GalNAc sulfate)2, hyaluronate tetrasaccharide (GlcUA-GlcNAc) 2 , methyl ß-Dglucuronyl-a-D-glucoside, and p-nitrophenyl /3-D-glucuronide proceeds at relative rates of 1.0:0.55:0.22:1.5. In the presence of 0.4M NaCl optimum hydrolysis shifts to pH 5.2 for the synthetic substrates, but natural substrates are not hydrolysed under these conditions. From the hydrolysis of hyaluronate and chondroitin sulfate saccharides and their chemical derivatives the following specificities of the ß-D -glucuronidase are derived: 0-D-Glucuronyl saccharides bearing non-sulfated A^-acetylhexosamine residue in preterminal position (disaccharides) are not hydrolysed by ß-D -glucuronidase unless an additional glucuronic residue occupies the last but two position of the substrate (trisaccharide). Sulfation of the internal TV-acetylhexosamine residue(s) enhances the rate of hydrolysis. In contrast to the nonhydrolysable ß-D -glucuronyl-./V-acetylgrucosamine (hyaluronate disaccharide), ]3-D-glucuronyl-anhydromannitol
Who reads Substrate Specificity and Regulation of Activity of Rat Liver β-D-Glucuronidase?
It is typically read by researchers, students, and practitioners in Biochemistry, Genetics and Molecular Biology.
- Author
- Reinhard NIEMANN; Eckhart BUDDECKE
- Publisher
- Walter de Gruyter GmbH
- Published
- 1982
- Language
- EN
- Field
- Biochemistry, Genetics and Molecular Biology (Life Sciences)